ArticleMolecular and cellular biology1999
NRIF3 is a novel coactivator mediating functional specificity of nuclear hormone receptors.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 65 citations in OpenAlex.
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- The Drosophila juvenile hormone receptor candidates methoprene-tolerant (MET) and germ cell-expressed (GCE) utilize a conserved LIXXL motif to bind the FTZ-F1 nuclear receptor.The Journal of biological chemistry · 2012Article
- Regulation of estrogen-dependent transcription by the LIM cofactors CLIM and RLIM in breast cancer.Cancer research · 2009Article
- Serine 28 phosphorylation of NRIF3 confers its co-activator function for estrogen receptor-alpha transactivation.Oncogene · 2008Article
- Nuclear receptor coactivator/coregulator NCoA6(NRC) is a pleiotropic coregulator involved in transcription, cell survival, growth and development.Nuclear receptor signaling · 2008Review
- Metastasis-associated protein 1 interacts with NRIF3, an estrogen-inducible nuclear receptor coregulator.Molecular and cellular biology · 2004Article
- The nuclear hormone receptor coactivator NRC is a pleiotropic modulator affecting growth, development, apoptosis, reproduction, and wound repair.Molecular and cellular biology · 2004Article
- The NRIF3 family of transcriptional coregulators induces rapid and profound apoptosis in breast cancer cells.Molecular and cellular biology · 2004Article
- PSF-TFE3 oncoprotein in papillary renal cell carcinoma inactivates TFE3 and p53 through cytoplasmic sequestration.Oncogene · 2003Article
- Discovery of diverse thyroid hormone receptor antagonists by high-throughput docking.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- NRC-interacting factor 1 is a novel cotransducer that interacts with and regulates the activity of the nuclear hormone receptor coactivator NRC.Molecular and cellular biology · 2002Article
- Functional evidence for retinoid X receptor (RXR) as a nonsilent partner in the thyroid hormone receptor/RXR heterodimer.Molecular and cellular biology · 2002Article
- Domain structure of the NRIF3 family of coregulators suggests potential dual roles in transcriptional regulation.Molecular and cellular biology · 2001Article
- Selective coactivation of estrogen-dependent transcription by CITED1 CBP/p300-binding protein.Genes & development · 2001Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Many nuclear receptors are capable of recognizing similar DNA elements. The molecular event(s) underlying the functional specificities of these receptors (in regulating the expression of their native target genes) is a very important issue that remains poorly understood. Here we report the cloning and analysis of a novel nuclear receptor coactivator (designated NRIF3) that exhibits a distinct receptor specificity. Fluorescence microscopy shows that NRIF3 localizes to the cell nucleus. The yeast two-hybrid and/or in vitro binding assays indicated that NRIF3 specifically interacts with the thyroid hormone receptor (TR) and retinoid X receptor (RXR) in a ligand-dependent fashion but does not bind to the retinoic acid receptor, vitamin D receptor, progesterone receptor, glucocorticoid receptor, or estrogen receptor. Functional experiments showed that NRIF3 significantly potentiates TR- and RXR-mediated transactivation in vivo but has little effect on other examined nuclear receptors. Domain and mutagenesis analyses indicated that a novel C-terminal domain in NRIF3 plays an essential role in its specific interaction with liganded TR and RXR while the N-terminal LXXLL motif plays a minor role in allowing optimum interaction. Computer modeling and subsequent experimental analysis suggested that the C-terminal domain of NRIF3 directly mediates interaction with liganded receptors through an LXXIL (a variant of the canonical LXXLL) module while the other part of the NRIF3 protein may still play a role in conferring its receptor specificity. Identification of a coactivator with such a unique receptor specificity may provide new insight into the molecular mechanism(s) of receptor-mediated transcriptional activation as well as the functional specificities of nuclear receptors.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.